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Information on EC 4.1.3.3 - N-acetylneuraminate lyase and Organism(s) Homo sapiens and UniProt Accession Q9BXD5

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.3 N-acetylneuraminate lyase
IUBMB Comments
This enzyme is involved in the degradation of N-acetylneuraminate. It is specific for the open form of the sugar. It also acts on N-glycoloylneuraminate and on O-acetylated sialic acids, other than 4-O-acetylated derivatives.
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This record set is specific for:
Homo sapiens
UNIPROT: Q9BXD5
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
n-acetylneuraminate lyase, sialic acid aldolase, n-acetylneuraminic acid aldolase, n-acetylneuraminic acid lyase, neu5ac aldolase, n-acetyl-d-neuraminic acid aldolase, neuac lyase, n-acetylneuraminate pyruvate lyase, neuraminic acid aldolase, n-acetylneuraminate pyruvate-lyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N-Acetylneuraminate lyase
-
Acetylneuraminate pyruvate-lyase
-
-
-
-
Lyase, acetylneuraminate
-
-
-
-
N-Acetylneuraminate aldolase
-
-
-
-
N-Acetylneuraminate lyase
-
-
-
-
N-acetylneuraminate pyruvate lyase
-
-
-
-
N-Acetylneuraminate pyruvate-lyase
-
-
-
-
N-Acetylneuraminic acid aldolase
-
-
-
-
N-Acetylneuraminic acid lyase
-
-
-
-
N-Acetylneuraminic aldolase
-
-
-
-
N-Acetylneuraminic lyase
-
-
-
-
NALase
-
-
-
-
NANA lyase
-
-
-
-
NeuAc aldolase
-
-
-
-
Neuraminate aldolase
-
-
-
-
Neuraminic acid aldolase
-
-
-
-
Neuraminic aldolase
-
-
-
-
NPL
-
-
-
-
sialate aldolase
-
-
Sialate lyase
-
-
-
-
sialate-pyruvate lyase
-
-
Sialic acid aldolase
-
-
-
-
Sialic aldolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-C-bond cleavage
-
condensation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
aceneuramate pyruvate-lyase (N-acetyl-D-mannosamine-forming)
This enzyme is involved in the degradation of N-acetylneuraminate. It is specific for the open form of the sugar. It also acts on N-glycoloylneuraminate and on O-acetylated sialic acids, other than 4-O-acetylated derivatives.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-60-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-deoxy-manno-oct-ulosonic acid
arabinose + pyruvate
show the reaction diagram
-
-
-
?
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
show the reaction diagram
-
-
-
?
N-Acetylneuraminic acid
N-Acetyl-D-mannosamine + pyruvate
show the reaction diagram
N-Glycolylneuraminic acid
?
show the reaction diagram
-
60% the rate of N-acetylneuraminic acid
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-acetylneuraminate
N-acetyl-D-mannosamine + pyruvate
show the reaction diagram
-
-
-
?
N-Acetylneuraminic acid
N-Acetyl-D-mannosamine + pyruvate
show the reaction diagram
-
regulation of sialic acid metabolism
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
-
36% inhibition after 15 min at 20°C
Hg2+
-
43% inhibition after 15 min at 20°C
pyruvate
-
36% inhibition at 1 mM, 65% inhibition at 5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4
N-acetylneuraminic acid
-
pH 7.4, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2
pyruvate
-
pH 7.4, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
peripheral blood
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NPL_HUMAN
320
0
35163
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Barbosa, J.A.R.G.; Smith, B.J.; DeGori, R.; Ooi, H.C.; Marcuccio, S.M.; Campi, E.M.; Jackson, W.R.; Brossmer, R.; Sommer, M.; Lawrence, M.C.
Active Site Modulation in the N-Acetylneuraminate Lyase Sub-family as Revealed by the Structure of the Inhibitor-complexed Haemophilus influenzae Enzyme
J. Mol. Biol.
303
405-421
2000
Haemophilus influenzae, Homo sapiens
Manually annotated by BRENDA team
Wu, M.; Gu, S.; Xu, J.; Zou, X.; Zheng, H.; Jin, Z.; Xie, Y.; Ji, C.; Mao, Y.
A novel splice variant of human gene NPL, mainly expressed in human liver, kidney and peripheral blood leukocyte
DNA Seq.
16
137-142
2005
Homo sapiens (Q9BXD5), Homo sapiens
Manually annotated by BRENDA team
Chu, H.Y.; Zheng, Q.C.; Zhao, Y.S.; Zhang, H.X.
Homology modeling and molecular dynamics study on N-acetylneuraminate lyase
J. Mol. Model.
15
323-328
2009
Homo sapiens (Q9BXD5), Homo sapiens
Manually annotated by BRENDA team